携带Lac+重组质粒的活动酵母菌发酵乳糖

Hideshi Yanase, Junn Kurii, Kenzo Tonomura
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引用次数: 11

摘要

引入了大肠杆菌β-半乳糖苷酶融合蛋白和乳糖渗透酶的Lac+重组质粒。融合蛋白的β-半乳糖苷酶活性为450 ~ 5860 Miller单位,具有乳糖酶功能。携带质粒的菌株比不携带质粒的菌株对棉子糖的吸收增强,表明乳糖渗透酶在生物体中起作用。携带质粒的Z. mobilis可以从乳糖和乳清中产生乙醇,但不能以乳糖为唯一碳源生长。结果发现,半乳糖或从乳糖中分离出来的半乳糖都能抑制这种生物的生长。
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Fermentation of lactose by Zymomonas mobilis carrying a Lac+ recombinant plasmid

Lac+ recombinant plasmids encoding a β-galactosidase fused protein and lactose permease of Escherichia coli were introduced Zymomonas mobilis. The fused protein was expressed with 450 to 5,860 Miller units of β-galactosidase activity, and functioned as lactase. Raffinose uptake by Z. mobilis CP4 was enhanced in the plasmid-carrying strain over the plasmid-free strain, suggesting that the lactose permease was functioning in the organism. Z. mobilis carrying the plasmid could produce ethanol from lactose and whey, but could not grow on lactose as the sole carbon source. It was found that the growth of the organism was inhibited by either galactose of the galactose liberated from lactose.

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